CN102120753A - Modified keratin material as well as preparation method and application thereof - Google Patents
Modified keratin material as well as preparation method and application thereof Download PDFInfo
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Abstract
The invention discloses a modified keratin material as well as a preparation method and application thereof. The modified keratin material provided by the invention has a structural formula shown in a formula (I) in the specification. The invention further provides the preparation method of the modified keratin material. The modified keratin material provided by the invention is degradable or degraded slowly after being implanted inside a human body, and the degradation degree of the modified keratin material can be regulated by controlling preparation process parameters. The prepared modified keratin material can be applied to hemostasis materials, hydrogel, wound dressing, and soft tissue fillers and the like, and can also be used as a support material for building a tissue engineered tissue.
Description
Technical field
The present invention relates to technical field of biomedical materials, be specifically related to a kind of modification keratin material and its production and application.
Background technology
Keratic research is mainly concentrated on extractive technique and performance study aspect both at home and abroad at present, seldom relate to the study on the modification of keratin material.
Generally speaking, the disulfide linkage in the keratin molecule makes and takes place crosslinkedly between peptide chain inside and the peptide chain, forms tridimensional network, makes natural keratin be difficult to dissolving, brings difficulty for keratic extraction in the hair, processing and application.Make that molecular weight is higher, solvability Keratin sulfate preferably, can only be by opened disulfide bond optionally, destroy method such as hydrogen bond and realize.Extracting keratic method at present roughly has mechanical process, chemical method and biological process etc., and wherein chemical method can be divided into acid and alkali hydrolysis method, reduction method and oxidation style etc. again.The application that often can mutually combine of other method and chemical method.The reaction conditions of reduction method is relatively gentleer, and less to the destructiveness of peptide chain, the Keratin sulfate molecular weight product of acquisition is higher, and productive rate is also higher, normally Shou Xuan chemical extraction method.
The common practices of the reduction method of domestic and international application is to handle feather or hair powder raw material with the urea soln of high density at present, so that Keratin sulfate swelling, add mercaptoethanol solution then and react extraction for some time at a certain temperature, the undissolved raw material of elimination, after ultrafiltration or dialysis treatment, centrifugation obtains keratin solution again; Or first centrifugation, from the supernatant liquid of centrifugation gained, separate out Keratin sulfate with salting-out process again, then this Keratin sulfate is dissolved in the mixed solution of ammoniacal liquor, water or water and lower alcohol, form keratin solution again.
At home and abroad in the document, used reductive agent is generally sulfhydryl compound, as Thioglycolic acid sodium salt, mercaptoethanol, Thiovanic acid and dithiothreitol dithio.Chemical property is stable in order to obtain, mechanical property keratin material preferably, and existing research report mainly is the effect by chemical cross-linking agent, to realize crosslinked between keratin molecule, strengthens degradation capability in the intensity of keratin material and the antibody.Linking agent commonly used is chemical substances such as glutaraldehyde, hexamethylene-diisocyanate, carbodiimide, (gathering) glycol dehydration glycerine ethers, epoxy chloropropane.These methods in the Keratin sulfate cross-linking process, exist introduce poisonous chemical ingredients, acid or alkali to keratic degraded, lack selectivity, crosslinking reaction irreversible, to bigger or the like the defective of keratin molecule structure deteriorate, have a strong impact on the application of Keratin sulfate as biomedical material.
Develop new keratin molecule modification technology and method, to reach under the reaction conditions of gentleness, the reagent that application security is higher, effectively keeping on keratin molecule constitutional features and the bioactive basis, realize keratin molecule effectively, reversible is cross-linking modified, and is as forming more disulfide linkage, better to form stability, more the novel keratin material that can regulate of difficult degradation or degradation rate has huge development prospect and application space.
Summary of the invention
The objective of the invention is to big according to the structure deteriorate that exists in the existing keratin molecule modified effect, crosslinking reaction is irreversible, lack selectivity, be easy to problem such as degraded, provide a kind of and be difficult to degrade and modification keratin material that palliating degradation degree can be regulated within the specific limits.
Another object of the present invention is to provide the preparation method of above-mentioned modification keratin material.
A further object of the invention is to provide the application of above-mentioned modification keratin material.
A kind of modification keratin material, its structural formula is suc as formula shown in (I): wherein, R1, R2 represent other amino-acid residue that links to each other with Serine, Threonine, tyrosine residues in the keratin molecule respectively; R5, R6 represent other amino-acid residue that links to each other with Methionin, arginine in the keratin molecule respectively; R3 represents the side group of Serine in the keratin molecule, Threonine or tyrosine residues; R4 represents the side group of Methionin in the keratin molecule, arginine residues; R7, R8 represent the sulfhydrylation modification group of the introducing that is connected on hydroxyl and the amino respectively; Upper left box is represented Serine, Threonine or tyrosine residues, and upper right box is represented Methionin, arginine residues, and on behalf of sulfhydrylation, lower frame modify the new disulfide linkage that forms in back.
Formula (I).
The basic ideas that the present invention prepares the modification keratin material are to adopt Guanidinium hydrochloride and Thiovanic acid as the Keratin sulfate extraction agent, extract preparation keratein(e) solution, utilize two (many) characteristics of functional groups of sulfhydrylization reagent simultaneously, with Serine in the keratin molecule chain, hydroxyl or Methionin in Threonine and the tyrosine side group, active amino in the arginine side group reacts, introduce the high-density sulfydryl, make the sulfydryl that generates except disulfide bond reduction in the rich thiolated modified keratin molecule of final formation, also increased the new sulfydryl of amino in the former keratin molecule chain upper amino acid residue and hydroxyl and sulfhydrylization reagent reaction back generation by Keratin sulfate self.So, the linked reaction by two (many) functional groups sulfhydrylization reagent has improved the sulfydryl density in the keratin molecule greatly, at last by oxidation, can generate a large amount of new disulfide linkage, and it is thiolated modified to reach keratic richness.
The preparation method of modification keratin material of the present invention comprises the steps:
(1) reduction of Keratin sulfate extraction and disulfide linkage;
(2) sulfhydrylation of keratin molecule is modified;
(3) sulfhydrylation is keratic oxidation cross-linked, obtains the modification keratin material.
As a kind of preferred version, sulfhydrylation described in the step (2) is modified and is comprised amino mercapto modification and the modification of hydroxyl sulfhydrylation; Used reagent was Thiovanic acid when described sulfhydrylation was modified, 2 mercaptopropionic acid, 3-thiohydracrylic acid, the D-halfcystine, L-halfcystine, sulfydryl butyric acid, mercaptoisobutyric acid, 2,3-dimercaptosuccinic acid and sodium salt thereof, sylvite, ammonium salt, 6-sulfydryl nicotinic acid, 2-amino-4-sulfydryl butyric acid, thiirane (thia cyclohexane), epithio propane (thiirane), the epithio chloropropane, Thietane and substitution product thereof or sulfydryl sodium.
Technical characterstic of the present invention is off the beaten track, in the keratein(e) solution that extracts, esterification or amidation or substitution reaction further take place by the active amino in the hydroxyl in Serine, Threonine and the tyrosine side group in two (many) functional group's sulfhydrylization reagents and the keratin molecule chain or Methionin, the arginine side group, thereby in keratin molecule, introduce new sulfydryl, promptly form rich sulfhydrylation Keratin sulfate.Natural oxidation by sulfydryl forms disulfide linkage between the modification keratin molecule at last, realizes the crosslinked of keratin molecule.The sharpest edges that prepare the modification keratin material by disulfide bond crosslinking are that can contain sulfhydryl reagent such as mercaptoethanol, Thiovanic acid, dithiothreitol dithio etc. by adding becomes the disulfide bond reduction in the modification keratin molecule free sulfhydryl groups again, promptly keraticly crosslinkedly can realize reversible crosslink.The dissolving power of Keratin sulfate in aqueous solvent strengthened, on the other hand, can utilize sulfydryl very easily the oxidation characteristics that form disulfide linkage realize in-situ cross-linkedly, promptly implanting earlier, it is crosslinked afterwards to realize.Do not need to add chemical cross-linking agent in this technical scheme simultaneously, do not introduce new impurity component, reduce purification step significantly, can expand the application of keratin material to a great extent in field of biomedical materials.
In the keratic preparation process of modification of the present invention, the Keratin sulfate of step (1) extracts and being reduced to of disulfide linkage:
R1 herein, R2 represent other amino-acid residue of linking to each other with halfcystine in the keratin molecule respectively.
Amino mercapto in the step (2) turns to:
R1 represents Methionin or the arginic side group in the keratin molecule herein, and other amino-acid residue of keratin molecule is formed in the R2 representative;
The hydroxyl sulfydryl turns to:
R1 represents the side group of Serine, Threonine or tyrosine in the keratin molecule herein, and other amino-acid residue of keratin molecule is formed in the R2 representative.
Sulfhydrylation in the step (3) is keratic oxidation cross-linkedly to be:
R1 represents the side group of Serine, Threonine or tyrosine in the keratin molecule in this formula, and R3 represents Methionin in the keratin molecule, arginine side group.R2, R4 represent other amino-acid residue of forming keratin molecule respectively.
In the above-mentioned steps, used catalyzer was 4-Dimethylamino pyridine, carbodiimide or N when described sulfhydrylation was modified, N '-carbonyl dimidazoles.
As a kind of most preferably scheme, in the above-mentioned preparation process, when sulfhydrylation was modified, the mass ratio of Keratin sulfate and sulfhydrylization reagent was 1:0.01 ~ 1:100; Temperature of reaction is a room temperature to 120 ℃; Reaction times is 1 ~ 48 hour; Catalyst levels accounts for 0.01 ~ 10% of reactant total mass.
In sum, the present invention is can be with the keratolysis in the hair by Thiovanic acid and Guanidinium hydrochloride, because above-mentioned two (many) functional groups of Thiovanic acid and other sulfhydrylization reagent can also react with the active amino in hydroxyl in Serine, Threonine and the tyrosine side group in the keratin molecule chain in the hair or Methionin, the arginine side group, introduces new sulfydryl.Because the sulfydryl that generates with hydroxyl in the corresponding amino-acid residue and amino reaction back is extra increasing, so after reacting with sulfhydrylization reagent, sulfhydryl content in the hair-keratin molecule increases considerably, after oxidation, sulfydryl forms disulfide linkage, make the keratin molecule crosslinking degree after the modification significantly increase, its chemical stability greatly strengthens, thereby can change Keratin sulfate biodegradable feature takes place easily, make it be suitable for can be used for hemostatic material as the long-term property implanted material in the body, hydrogel, wound dressing, soft tissue is filled or as the timbering material of engineered tissue construction.
Compared with prior art, the present invention has following beneficial effect:
(1) modification keratin material of the present invention is a kind of novel insoluble or than keratin material difficult degradation or that degradation rate can be regulated;
(2) preparation method of modification keratin material of the present invention is simple, does not need to carry out complicated chemical reaction, can accomplish scale production;
(3) preparation method of modification keratin material of the present invention adopts two (many) molecule of functional group contain sulfydryl as modifying agent, do not adopt in the modifying process poisonous, have pungency maybe may produce dysgenic solvent or other chemical reagent to human body;
(4) the present invention carries out modification by introducing highdensity sulfydryl to keratein(e), prepares rich sulfhydrylation keratin material
(5) the present invention produces the high-density disulfide linkage by the keratein(e) of the rich sulfhydrylation of oxygen/air oxidation, realizes the crosslinked of keratin molecule, and the Keratin sulfate after the while is crosslinked can become soluble keratin with reductive agent again, and promptly this cross-linking process is reversible;
(6) the present invention does not change application feature in keratic basic chemical property and the body, can improve keratic stability simultaneously, reaches physiological environment indissoluble or insoluble in vivo, significantly improves its degradation resistant ability, realizes the function of the long-term property implanted.
Embodiment
Further explain the present invention below in conjunction with embodiment, but embodiment does not do any type of qualification to the present invention.
Embodiment 1
(1) get the human hair, use surfactant washing, deionized water is rinsed well repeatedly, dries in 80 ℃ of baking ovens.
(2) apparatus,Soxhlet's of packing into, 1:1 ethanol ether mixed solvent degreasing 6h, deionized water rinsing drying for standby repeatedly.
(3) people after the clean degreasing sends out and is soaked in 30% hydrogen peroxide and the strong aqua mixing solutions (volume ratio 3:1), keeps 1h under the room temperature, the people is distributed remove pigment entirely.Again through washing and drying.
(4) solution of preparation Thiovanic acid 0.2mol/L and Guanidinium hydrochloride 6mol/l.The descendant sends out sample through skimming treatment, and be soaked in according to mass ratio 1:100 and extract in the solution, soaking at room temperature 2h, 50 ℃ are reacted 12h down.
(5) centrifugation behind the extracting liquid filtering, filtrate is that 12 ~ 14KD dialysis membrane is dialysed about 36h to water through holding back relative molecular mass, obtains water white transparency keratein(e) solution.
(6) keratin solution gets the Keratin sulfate powder through concentrating postlyophilization.
(7) the Keratin sulfate powder is dissolved in the Thiovanic acid solution of 0.5mol/l again, adds an amount of 4-Dimethylamino pyridine as catalyzer, and 55 ℃ are reacted 2h down, get the sulfhydrylation keratin solution.
(8) the sulfhydrylation keratin solution according to step (5) dialysis treatment, obtains purified sulfhydrylation keratin solution once more.
(9) the sulfhydrylation keratin solution aerating oxygen under room temperature after purified forms white flocculent precipitate until Keratin sulfate and separates from solution.Obtain the Keratin sulfate gel.
(10) the Keratin sulfate gel obtains the crosslinked Keratin sulfate powder that is rich in disulfide linkage of white through lyophilize.
Embodiment 2
(1) get the people and send out, detergent immersion cleans, and deionized water is rinsed well repeatedly, dries in 80 ℃ of baking ovens.
(2) distilling flask of packing into adds and accounts for the chloroform that the people sends out 10 times of quality, reflux extraction, and degreasing 4h isolates chloroform, adds the acetone of 10 times of quality, and behind the stirring at room 1h, filtering acetone is sent out sample with deionized water rinsing drying for standby repeatedly.
(3) people after degreasing is cleaned sends out and is soaked in 30% hydrogen peroxide, keeps 3h under the room temperature, the people is distributed remove pigment entirely.Again through washing and drying.
(4) solution of preparation mercaptoethanol 0.5mol/L and Guanidinium hydrochloride 8mol/l.
(5) send out sample through the skimming treatment descendant, be soaked in according to mass ratio 1:100 and extract in the solution, behind the soaking at room temperature 2h, 60 ℃ are reacted 12h down.
(6) centrifugation behind the extracting liquid filtering, filtrate through hold back relative molecular mass be 12 ~ 14KD ultra-filtration membrane ultrafiltration and concentration to 1/3 of raw sample volume, obtain water white transparency keratein(e) solution.
(7) add the deionized water of 10 times of volumes again, continue ultrafiltration and concentration to 1/10 volume, the concentrated solution lyophilize, the Keratin sulfate powder.
(8) the Keratin sulfate powder is dissolved in the thiohydracrylic acid solution of 2.0mol/l again, adds an amount of 4-Dimethylamino pyridine as catalyzer, and 70 ℃ are reacted 1h down, get the sulfhydrylation keratin solution.
(9) the sulfhydrylation keratin solution according to step (6,7) uf processing, obtains purified sulfhydrylation keratin solution once more.
(10) the sulfhydrylation keratin solution aerating oxygen under room temperature after purified forms white flocculent precipitate until Keratin sulfate and separates from solution.Obtain the Keratin sulfate gel.
(11) the Keratin sulfate gel obtains the crosslinked Keratin sulfate powder that is rich in disulfide linkage of white through lyophilize.
Claims (8)
1. modification keratin material, it is characterized in that its structural formula is suc as formula shown in (I): wherein, R1, R2 represent other amino-acid residue that links to each other with Serine, Threonine, tyrosine residues in the keratin molecule respectively; R5, R6 represent other amino-acid residue that links to each other with Methionin, arginine in the keratin molecule respectively; R3 represents the side group of Serine in the keratin molecule, Threonine or tyrosine residues; R4 represents the side group of Methionin in the keratin molecule, arginine residues; R7, R8 represent the sulfhydrylation modification group of the introducing that is connected on hydroxyl and the amino respectively; Upper left box is represented Serine, Threonine or tyrosine residues, and upper right box is represented Methionin, arginine residues, and on behalf of sulfhydrylation, lower frame modify the new disulfide linkage that forms in back;
Formula (I).
2. the preparation method of the described modification keratin material of claim 1 is characterized in that comprising the steps:
(1) reduction of Keratin sulfate extraction and disulfide linkage;
(2) sulfhydrylation of keratin molecule is modified;
(3) sulfhydrylation is keratic oxidation cross-linked, obtains the modification keratin material.
3. according to the preparation method of the described modification keratin material of claim 2, it is characterized in that described sulfhydrylation modification comprises amino mercapto modification and the modification of hydroxyl sulfhydrylation.
4. according to the preparation method of the described modification keratin material of claim 3, it is characterized in that described sulfhydrylation is that the active amino in the hydroxyl in Serine, Threonine and the tyrosine side group in the keratin molecule chain or Methionin, the arginine side group is reacted, introduce highdensity new sulfydryl, finally form rich thiolated modified Keratin sulfate.
5. the preparation method of modification keratin material according to claim 2, used reagent is Thiovanic acid when it is characterized in that described sulfhydrylation is modified, 2 mercaptopropionic acid, the 3-thiohydracrylic acid, the D-halfcystine, the L-halfcystine, sulfydryl butyric acid, mercaptoisobutyric acid, 2,3-dimercaptosuccinic acid and sodium salt thereof, sylvite, ammonium salt, 6-sulfydryl nicotinic acid, 2-amino-4-sulfydryl butyric acid, thiirane (thia cyclohexane), epithio propane (thiirane), epithio chloropropane, Thietane and substitution product thereof or sulfydryl sodium.
6. the preparation method of modification keratin material according to claim 4, used catalyzer is 4-Dimethylamino pyridine, carbodiimide or N when it is characterized in that described sulfhydrylation is modified, N '-carbonyl dimidazoles.
7. the preparation method of modification keratin material according to claim 6, when it is characterized in that sulfhydrylation is modified, the mass ratio of Keratin sulfate and sulfhydrylization reagent is 1:0.01 ~ 1:100; Temperature of reaction is a room temperature to 120 ℃; Reaction times is 1 ~ 48 hour; Catalyst levels accounts for 0.01 ~ 10% of reactant total mass.
8. the described modification keratin material of claim 1 is at hemostatic material, hydrogel, wound dressing, soft tissue filling material or as the application in the timbering material of engineered tissue construction.
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| CN102492166A (en) * | 2011-11-24 | 2012-06-13 | 东华大学 | Method for preparing feather keratin sponge by using feathers |
| CN102504503A (en) * | 2011-09-29 | 2012-06-20 | 广州卓扬新材料科技有限公司 | Full-biodegradation ceratin fiber reinforced and fireproof modified polylactic acid material and preparation method thereof |
| EP2916812A4 (en) * | 2012-11-06 | 2016-07-27 | Keranetics Llc | White keratin compositions |
| CN107043467A (en) * | 2017-06-02 | 2017-08-15 | 东华大学 | A kind of Photocrosslinkable hydrogel and preparation method thereof |
| CN108714243A (en) * | 2017-06-08 | 2018-10-30 | 重庆大学 | Implant and preparation method thereof for post operation of hypertensive cerebral hemorrhage hemostasis |
| CN109481726A (en) * | 2018-11-26 | 2019-03-19 | 广州新诚生物科技有限公司 | A kind of biodegradable hemostasis bone wax and preparation method thereof |
| US10279045B2 (en) | 2011-08-17 | 2019-05-07 | Keranetics Llc | Low protein percentage gelling compositions |
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| US10385095B2 (en) | 2011-08-17 | 2019-08-20 | Keratin Biosciences, Inc | Methods for extracting keratin proteins |
| CN110699855A (en) * | 2019-11-08 | 2020-01-17 | 南通大学 | Preparation method of conductive chitosan/keratin nanofiber membrane |
| CN111535038A (en) * | 2020-06-09 | 2020-08-14 | 湖州市练市新民纺织有限公司 | Preparation process of anti-pilling worsted wool yarn |
| US10792239B2 (en) | 2012-11-06 | 2020-10-06 | Kernnetics, Inc. | White keratin compositions |
| CN114108360A (en) * | 2021-11-24 | 2022-03-01 | 安徽工程大学 | Waste feather-based heat-preservation sound-absorption material and preparation method thereof |
| CN116655939A (en) * | 2023-06-05 | 2023-08-29 | 西安工程大学 | Keratin regenerated material with mercapto/disulfide bond dynamic covalent crosslinking system and preparation method thereof |
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| US11034722B2 (en) | 2011-08-17 | 2021-06-15 | KeraNetics, Inc. | Methods for extracting keratin proteins |
| US10385095B2 (en) | 2011-08-17 | 2019-08-20 | Keratin Biosciences, Inc | Methods for extracting keratin proteins |
| US10709789B2 (en) | 2011-08-17 | 2020-07-14 | KeraNetics, Inc. | Low protein percentage gelling compositions |
| US10279045B2 (en) | 2011-08-17 | 2019-05-07 | Keranetics Llc | Low protein percentage gelling compositions |
| CN102504503A (en) * | 2011-09-29 | 2012-06-20 | 广州卓扬新材料科技有限公司 | Full-biodegradation ceratin fiber reinforced and fireproof modified polylactic acid material and preparation method thereof |
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| EP2916812A4 (en) * | 2012-11-06 | 2016-07-27 | Keranetics Llc | White keratin compositions |
| US10792239B2 (en) | 2012-11-06 | 2020-10-06 | Kernnetics, Inc. | White keratin compositions |
| CN107043467A (en) * | 2017-06-02 | 2017-08-15 | 东华大学 | A kind of Photocrosslinkable hydrogel and preparation method thereof |
| CN108714243A (en) * | 2017-06-08 | 2018-10-30 | 重庆大学 | Implant and preparation method thereof for post operation of hypertensive cerebral hemorrhage hemostasis |
| CN109481726A (en) * | 2018-11-26 | 2019-03-19 | 广州新诚生物科技有限公司 | A kind of biodegradable hemostasis bone wax and preparation method thereof |
| CN109735949A (en) * | 2019-01-12 | 2019-05-10 | 太原理工大学 | A kind of anti-ultraviolet wet absorption fever protein tencel fiber and preparation method thereof |
| CN109735949B (en) * | 2019-01-12 | 2021-07-30 | 山西瑞赛格纺织科技有限公司 | Ultraviolet-resistant, moisture-absorbing and heating protein tencel fiber and preparation method thereof |
| CN110699855A (en) * | 2019-11-08 | 2020-01-17 | 南通大学 | Preparation method of conductive chitosan/keratin nanofiber membrane |
| CN110699855B (en) * | 2019-11-08 | 2021-09-10 | 南通大学 | Preparation method of conductive chitosan/keratin nanofiber membrane |
| CN111535038A (en) * | 2020-06-09 | 2020-08-14 | 湖州市练市新民纺织有限公司 | Preparation process of anti-pilling worsted wool yarn |
| CN114108360A (en) * | 2021-11-24 | 2022-03-01 | 安徽工程大学 | Waste feather-based heat-preservation sound-absorption material and preparation method thereof |
| CN114108360B (en) * | 2021-11-24 | 2022-08-05 | 安徽工程大学 | Waste feather-based heat-preservation sound-absorption material and preparation method thereof |
| CN116655939A (en) * | 2023-06-05 | 2023-08-29 | 西安工程大学 | Keratin regenerated material with mercapto/disulfide bond dynamic covalent crosslinking system and preparation method thereof |
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